The Zeaxanthin-Independent and Zeaxanthin-Dependent qE Components of Nonphotochemical Quenching Involve Common Conformational Changes within the Photosystem II Antenna in Arabidopsis

Johnson, Matthew P.; Pérez-Bueno, María Luisa; Zia, Ahmad; Horton, Peter; Ruban, Alexander V.

doi:10.1104/pp.108.129957

Cited by 135 publications

(157 citation statements)

References 70 publications

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“…Different from LHCII, in which the binding of zeaxanthin in the internal sites leads to a destabilization of the complex (30) and to a strong decrease of the triplet quenching efficiency (50), in CP24 the presence of zeaxanthin in the L2 site does not destabilize the complex and ensure a triplet quenching identical to the WT. This supports the idea of a different role of CP24 and LHCII in vivo, where CP24, but not LHCII, is expected to be able to exchange violaxanthin for zeaxanthin in the L2 site during the activity of the xanthophyll cycle (62), thus participating to the zeaxanthin-dependent quenching (63).…”

Section: Role Of Individual Pigments In Light Harvesting and Photoprosupporting

confidence: 66%

Molecular Basis of Light Harvesting and Photoprotection in CP24

Passarini

Wientjes

Hienerwadel

et al. 2009

Journal of Biological Chemistry

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CP24 is a minor antenna complex of Photosystem II, which is specific for land plants. It has been proposed that this complex is involved in the process of excess energy dissipation, which protects plants from photodamage in high light conditions. Here, we have investigated the functional architecture of the complex, integrating mutation analysis with time-resolved spectroscopy. A comprehensive picture is obtained about the nature, the spectroscopic properties, and the role in the quenching in solution of the pigments in the individual binding sites. The lowest energy absorption band in the chlorophyll a region corresponds to chlorophylls 611/612, and it is not the site of quenching in CP24. Chlorophylls 613 and 614, which are present in the major lightharvesting complex of Photosystem appear to be absent in CP24. In contrast to all other light-harvesting complexes, CP24 is stable when the L1 carotenoid binding site is empty and upon mutations in the third helix, whereas mutations in the first helix strongly affect the folding/stability of the pigment-protein complex. The absence of lutein in L1 site does not have any effect on the quenching, whereas substitution of violaxanthin in the L2 site with lutein or zeaxanthin results in a complex with enhanced quenched fluorescence. Triplet-minus-singlet measurements indicate that zeaxanthin and lutein in site L2 are located closer to chlorophylls than violaxanthin, thus suggesting that they can act as direct quenchers via a strong interaction with a neighboring chlorophyll. The results provide the molecular basis for the zeaxanthin-dependent quenching in isolated CP24.

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Section: Role Of Individual Pigments In Light Harvesting and Photoprosupporting

confidence: 66%

Molecular Basis of Light Harvesting and Photoprotection in CP24

Passarini

Wientjes

Hienerwadel

et al. 2009

Journal of Biological Chemistry

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“…The light-saturated capacity for NPQ DL in similar experiments was approximately 80 per cent of that of NPQ DLAZ , and approximately 35 per cent greater than NPQ DpH attained in the absence of xanthophyll de-epoxidation [25]. Although xanthophyll-dependent and independent forms of NPQ may share a common mechanism [47], it is unclear at the physiological level how these capacities relate; does NPQ DLAZ for example, substitute for NPQ DpH or is it simply additive?…”

Section: Resultsmentioning

confidence: 95%

From ecophysiology to phenomics: some implications of photoprotection and shade–sun acclimation in situ for dynamics of thylakoids in vitro

Matsubara

Förster

Waterman

et al. 2012

Phil. Trans. R. Soc. B

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Half a century of research into the physiology and biochemistry of sun-shade acclimation in diverse plants has provided reality checks for contemporary understanding of thylakoid membrane dynamics. This paper reviews recent insights into photosynthetic efficiency and photoprotection from studies of two xanthophyll cycles in old shade leaves from the inner canopy of the tropical trees Inga sapindoides and Persea americana (avocado). It then presents new physiological data from avocado on the time frames of the slow coordinated photosynthetic development of sink leaves in sunlight and on the slow renovation of photosynthetic properties in old leaves during sun to shade and shade to sun acclimation. In so doing, it grapples with issues in vivo that seem relevant to our increasingly sophisticated understanding of DpH-dependent, xanthophyll-pigment-stabilized non-photochemical quenching in the antenna of PSII in thylakoid membranes in vitro.

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“…Comparing two-photon Chl fluorescence with fluorescence upon direct one-photon Chl excitation allows quantification of the electronic interaction between Cars and Chls (38). In isolated LHCII, as well as in intact plants, this interaction corre- Ϫ1 band (full width at half maximum ϭ 6 -7 cm Ϫ1 ) assigned to H bond formation (18,20). Quenching in gels was 91%.…”

Section: Do These Changes Exist In Wt Lhciimentioning

confidence: 99%

“…The formation of NPQ is also associated with certain absorption changes that have been suggested to reflect a conformational change in LHCII, brought about by its protonation. The light Ϫ dark recovery absorption difference spectrum is characterized by a series of positive and negative bands, the best-known of which is ⌬A535 (20). Using resonance Raman the origin of ⌬A535 was shown to be a sub-population of red-shifted zeaxanthin molecules (21).…”

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confidence: 99%

Photoprotection in Plants Involves a Change in Lutein 1 Binding Domain in the Major Light-harvesting Complex of Photosystem II

Ilioaia

Johnson

Liao

et al. 2011

Journal of Biological Chemistry

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Nonphotochemical quenching (NPQ) is the fundamental process by which plants exposed to high light intensities dissipate the potentially harmful excess energy as heat. Recently, it has been shown that efficient energy dissipation can be induced in the major light-harvesting complexes of photosystem II (LHCII) in the absence of protein-protein interactions. Spectroscopic measurements on these samples (LHCII gels) in the quenched state revealed specific alterations in the absorption and circular dichroism bands assigned to neoxanthin and lutein 1 molecules. In this work, we investigate the changes in conformation of the pigments involved in NPQ using resonance Raman spectroscopy. By selective excitation we show that, as well as the twisting of neoxanthin that has been reported previously, the lutein 1 pigment also undergoes a significant change in conformation when LHCII switches to the energy dissipative state. Selective two-photon excitation of carotenoid (Car) dark states (Car S 1 ) performed on LHCII gels shows that the extent of electronic interactions between Car S 1 and chlorophyll states correlates linearly with chlorophyll fluorescence quenching, as observed previously for isolated LHCII (aggregated versus trimeric) and whole plants (with versus without NPQ).The photosynthetic process starts with the absorption of incoming solar photons by specialized pigment-protein complexes. In plants, light energy is absorbed by the two multisubunit protein-cofactor complexes, photosystem I (PSI) 3 and photosystem II (PSII), and the excitation energy is efficiently transferred to their reaction centers where photochemistry takes place. When these organisms are in low light environments, the process of light energy collection is extremely efficient. However, this process is regulated when the incoming light energy is above that which can be used in electron transport. In these latter conditions, the light-harvesting antenna is able to switch into a photoprotective mode, dissipating the excess energy as heat (1-3). This regulatory mechanism is measured as nonphotochemical quenching of chlorophyll (Chl) fluorescence (NPQ). In higher plants NPQ is a multicomponent process whose major component is called qE (energy-dependent quenching) (4), dependent upon the formation of the proton gradient (⌬pH) across the thylakoid membrane (which itself results from photosynthetic activity) (5). qE is facilitated by the deepoxidation of violaxanthin to zeaxanthin in the xanthophyll cycle (6). The PsbS protein also plays a crucial role in this process, possibly acting as a pH sensor (7,8). A key characteristic of the qE process is that it is induced in seconds and thus cannot involve de novo protein synthesis, but rather corresponds to a reorganization of the existing photosynthetic architecture.In the past decade a large amount of work has been performed to gain insight in the molecular mechanism(s) underlying this process, and several hypotheses have been put forward (9 -12). Among these, it was in particular proposed that excitation e...

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The Zeaxanthin-Independent and Zeaxanthin-Dependent qE Components of Nonphotochemical Quenching Involve Common Conformational Changes within the Photosystem II Antenna in Arabidopsis

Cited by 135 publications

References 70 publications

Molecular Basis of Light Harvesting and Photoprotection in CP24

Molecular Basis of Light Harvesting and Photoprotection in CP24

From ecophysiology to phenomics: some implications of photoprotection and shade–sun acclimation in situ for dynamics of thylakoids in vitro

Photoprotection in Plants Involves a Change in Lutein 1 Binding Domain in the Major Light-harvesting Complex of Photosystem II

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